6fvu: Difference between revisions
New page: '''Unreleased structure''' The entry 6fvu is ON HOLD Authors: Eisele, M.R., Reed, R.G., Rudack, T., Schweitzer, A., Beck, F., Nagy, I., Pfeifer, G., Plitzko, J.M., Baumeister, W., Tomko... |
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The entry | ==26S proteasome, s2 state== | ||
<SX load='6fvu' size='340' side='right' viewer='molstar' caption='[[6fvu]], [[Resolution|resolution]] 4.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6fvu]] is a 19 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FVU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FVU FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6fvu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fvu OCA], [https://pdbe.org/6fvu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fvu RCSB], [https://www.ebi.ac.uk/pdbsum/6fvu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fvu ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PSA4_YEAST PSA4_YEAST] The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The proteasome is the central protease for intracellular protein breakdown. Coordinated binding and hydrolysis of ATP by the six proteasomal ATPase subunits induces conformational changes that drive the unfolding and translocation of substrates into the proteolytic 20S core particle for degradation. Here, we combine genetic and biochemical approaches with cryo-electron microscopy and integrative modeling to dissect the relationship between individual nucleotide binding events and proteasome conformational dynamics. We demonstrate unique impacts of ATP binding by individual ATPases on the proteasome conformational distribution and report two conformational states of the proteasome suggestive of a rotary ATP hydrolysis mechanism. These structures, coupled with functional analyses, reveal key roles for the ATPases Rpt1 and Rpt6 in gating substrate entry into the core particle. This deepened knowledge of proteasome conformational dynamics reveals key elements of intersubunit communication within the proteasome and clarifies the regulation of substrate entry into the proteolytic chamber. | |||
Expanded Coverage of the 26S Proteasome Conformational Landscape Reveals Mechanisms of Peptidase Gating.,Eisele MR, Reed RG, Rudack T, Schweitzer A, Beck F, Nagy I, Pfeifer G, Plitzko JM, Baumeister W, Tomko RJ Jr, Sakata E Cell Rep. 2018 Jul 31;24(5):1301-1315.e5. doi: 10.1016/j.celrep.2018.07.004. PMID:30067984<ref>PMID:30067984</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6fvu" style="background-color:#fffaf0;"></div> | ||
[[Category: Beck | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Proteasome 3D structures|Proteasome 3D structures]] | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: Rudack | </SX> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Saccharomyces cerevisiae S288C]] | ||
[[Category: | [[Category: Baumeister W]] | ||
[[Category: Beck F]] | |||
[[Category: Eisele MR]] | |||
[[Category: Nagy I]] | |||
[[Category: Pfeifer G]] | |||
[[Category: Plitzko JM]] | |||
[[Category: Reed RG]] | |||
[[Category: Rudack T]] | |||
[[Category: Sakata E]] | |||
[[Category: Schweitzer A]] | |||
[[Category: Tomko RJ]] | |||